Abstract
ThepurA gene ofThiobacillus ferrooxidans encoding adenylosuccinate synthetase [EC 6.3.4.4] was identified in the upstream region of theiro gene encoding Fe(II)-oxidase (J. Biol. Chem 267:11242–11247, 1992). ThepurA gene consisted of 1290 base-pairs, which translated into a 29-amino-acid protein. The gene is functionally active, because it is able to complement anEscherichia coli purA-deficient strain. The deduced gene product has a high degree (60.9%) of sequence identity with that (432 aa) ofE. coli purA gene, and both the products share GDEGKGK-DETG-TKLD sequences which are supposed to be GTP-binding domain. The downstream region of theiro gene contained another open-reading frame (ORF) of 1218 bp, and this showed high homlogy (56.6% over 249 bp) withE. coli ORF-II, which is found as a second ORF and truncated form in the downstream region of thepurA gene. Comparison of the gene organization in the flanking region ofpurA gene betweenT. ferrooxidans andE. coli is also described.
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Kusano, T., Takeshima, T., Inoue, C. et al. Identification of thepurA gene encoding adenylosuccinate synthetase inThiobacillus ferrooxidans . Current Microbiology 26, 197–204 (1993). https://doi.org/10.1007/BF01577377
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DOI: https://doi.org/10.1007/BF01577377